8ur4
Crystal Structure of macrophage migration inhibitory factor (MIF) from Trichomonas vaginalis (I4122 form)Crystal Structure of macrophage migration inhibitory factor (MIF) from Trichomonas vaginalis (I4122 form)
Structural highlights
Publication Abstract from PubMedThe unicellular parasitic protozoan Trichomonas vaginalis causes trichomoniasis, the most prevalent nonviral sexually transmitted disease globally. T. vaginalis evades host immune responses by producing homologs of host proteins, including cytokines such as macrophage migration inhibitory factor. T. vaginalis macrophage migration inhibitory factor (TvMIF) helps to facilitate the survival of T. vaginalis during nutritional stress conditions, increases prostate cell proliferation and invasiveness, and induces inflammation-related cellular pathways, thus mimicking the ability of human MIF to increase inflammation and cell proliferation. The production, crystallization and three structures of N-terminally hexahistidine-tagged TvMIF reveal a prototypical MIF trimer with a topology similar to that of human homologs (hMIF-1 and hMIF-2). The N-terminal tag obscures the expected pyruvate-binding site. The similarity of TvMIF to its human homologs can be exploited for structure-based drug discovery. Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.,Srivastava A, Nair A, Dawson OCO, Gao R, Liu L, Craig JK, Battaile KP, Harmon EK, Barrett LK, Van Voorhis WC, Subramanian S, Myler PJ, Lovell S, Asojo OA, Darwiche R Acta Crystallogr F Struct Biol Commun. 2024 Dec 1;80(Pt 12):341-7. doi: , 10.1107/S2053230X24011105. PMID:39601418[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||